1BUW
CRYSTAL STRUCTURE OF S-NITROSO-NITROSYL HUMAN HEMOGLOBIN A
Summary for 1BUW
| Entry DOI | 10.2210/pdb1buw/pdb |
| Descriptor | PROTEIN (HEMOGLOBIN), PROTOPORPHYRIN IX CONTAINING FE, NITRIC OXIDE, ... (5 entities in total) |
| Functional Keywords | oxygen transport and vasodilation, oxygen storage-transport complex, oxygen storage/transport |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 64725.07 |
| Authors | Chan, N.-L.,Rogers, P.H.,Arnone, A. (deposition date: 1998-09-06, release date: 1998-09-16, Last modification date: 2024-10-30) |
| Primary citation | Chan, N.L.,Rogers, P.H.,Arnone, A. Crystal structure of the S-nitroso form of liganded human hemoglobin. Biochemistry, 37:16459-16464, 1998 Cited by PubMed Abstract: Although numerous reports have documented that the S-nitrosylation of cysteine residues by NO alters the activities of a wide variety of proteins, the direct visualization and the structural consequences of this reversible modification have not yet been reported for any protein. Here we describe the crystal structure of S-nitroso-nitrosylhemoglobin determined at a resolution of 1.8 A. The specific reaction of NO with Cys93beta is confirmed in this structure, and a large S-nitrosylation-induced change in the tertiary structure of the COOH-terminal dipeptides of the beta subunits provides additional insight into the stereochemical mechanism by which blood flow is regulated by the interaction of NO with hemoglobin. PubMed: 9843411DOI: 10.1021/bi9816711 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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